TGFβ signalling acts as a molecular brake of myoblast fusion

Julie Melendez, Daniel Sieiro, David Salgado, Valérie Morin, Marie-Julie Dejardin, Chan Zhou, Alan C. Mullen and Christophe Marcelle ()
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Julie Melendez: University Claude Bernard Lyon1, CNRS UMR 5310, INSERM U1217
Daniel Sieiro: University Claude Bernard Lyon1, CNRS UMR 5310, INSERM U1217
David Salgado: Monash University
Valérie Morin: University Claude Bernard Lyon1, CNRS UMR 5310, INSERM U1217
Marie-Julie Dejardin: University Claude Bernard Lyon1, CNRS UMR 5310, INSERM U1217
Chan Zhou: Massachusetts General Hospital
Alan C. Mullen: Harvard Stem Cell Institute
Christophe Marcelle: University Claude Bernard Lyon1, CNRS UMR 5310, INSERM U1217

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: Abstract Fusion of nascent myoblasts to pre-existing myofibres is critical for skeletal muscle growth and repair. The vast majority of molecules known to regulate myoblast fusion are necessary in this process. Here, we uncover, through high-throughput in vitro assays and in vivo studies in the chicken embryo, that TGFβ (SMAD2/3-dependent) signalling acts specifically and uniquely as a molecular brake on muscle fusion. While constitutive activation of the pathway arrests fusion, its inhibition leads to a striking over-fusion phenotype. This dynamic control of TGFβ signalling in the embryonic muscle relies on a receptor complementation mechanism, prompted by the merging of myoblasts with myofibres, each carrying one component of the heterodimer receptor complex. The competence of myofibres to fuse is likely restored through endocytic degradation of activated receptors. Altogether, this study shows that muscle fusion relies on TGFβ signalling to regulate its pace.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20290-1

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DOI: 10.1038/s41467-020-20290-1

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